Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum.

Molecular biology of the cell - 1 Feb 1992

Stirling C J, Rothblatt J, Hosobuchi M, Deshaies R, Schekman R

Abstract excerpt

Yeast mutants defective in the translocation of soluble secretory proteins into the lumen of the endoplasmic reticulum (sec61, sec62, sec63) are not impaired in the assembly and glycosylation of the type II membrane protein dipeptidylaminopeptidase B (DPAPB) or of a chimeric membrane protein consisting of the multiple membrane-spanning domain of yeast hydroxymethylglutaryl CoA reductase (HMG1) fused to yeast...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Division

Share to Cloning, Molecular

Share to Fungal Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 1550957
DOI: 10.1091/mbc.3.2.129
PMCID: PMC275513

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum.PMID 1550957Read ↗

Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Semantic proximity Read ↗

Cloning of the Pichia anomala SEC61 gene and its expression in a Saccharomyces cerevisiae sec61 mutant.Semantic proximity Read ↗

Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus.Semantic proximity Read ↗

Distinct domains within yeast Sec61p involved in post-translational translocation and protein dislocation.Semantic proximity Read ↗

Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae.Semantic proximity Read ↗

New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex.Semantic proximity Read ↗

The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons.Semantic proximity Read ↗

Characterization of the Saccharomyces cerevisiae sec6-4 mutation and tools to create S. cerevisiae strains containing the sec6-4 allele.Semantic proximity Read ↗

Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae.Semantic proximity Read ↗

Cancer associated mutations in Sec61γ alter the permeability of the ER translocase.Semantic proximity Read ↗

The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.Semantic proximity Read ↗

The exocyst subunit Sec3 is regulated by a protein quality control pathway.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.